KTI12_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KTI12_HUMAN
• UniProt AC: Q96EK9
• Protein Name: Protein KTI12 homolog
• Gene Name: KTI12
• Organism: Homo sapiens (Human).
• Sequence Length: 354
• Protein Sequence: MPLVVFCGLPYSGKSRRAEELRVALAAEGRAVYVVDDAAVLGAEDPAVYGDSAREKALRGALRASVERRLSRHDVVILDSLNYIKGFRYELYCLARAARTPLCLVYCVRPGGPIAGPQVAGANENPGRNVSVSWRPRAEEDGRAQAAGSSVLRELHTADSVVNGSAQADVPKELEREESGAAESPALVTPDSEKSAKHGSGAFYSPELLEALTLRFEAPDSRNRWDRPLFTLVGLEEPLPLAGIRSALFENRAPPPHQSTQSQPLASGSFLHQLDQVTSQVLAGLMEAQKSAVPGDLLTLPGTTEHLRFTRPLTMAELSRLRRQFISYTKMHPNNENLPQLANMFLQYLSQSLH

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Ubiquitination	CGLPYSGKSRRAEEL ECCCCCCCCCCHHHH	34.54	22505724
65	Phosphorylation	LRGALRASVERRLSR HHHHHHHHHHHHHHC	20.34	27067055
71	Phosphorylation	ASVERRLSRHDVVIL HHHHHHHHCCCEEEE	26.26	-
92	Phosphorylation	KGFRYELYCLARAAR CCCHHHHHHHHHHHC	3.57	-
96	Methylation	YELYCLARAARTPLC HHHHHHHHHHCCCEE	18.81	115481443
99	Methylation	YCLARAARTPLCLVY HHHHHHHCCCEEEEE	35.57	115481451
103	S-palmitoylation	RAARTPLCLVYCVRP HHHCCCEEEEEEECC	2.25	29575903
107	S-palmitoylation	TPLCLVYCVRPGGPI CCEEEEEEECCCCCC	1.31	29575903
131	Phosphorylation	ENPGRNVSVSWRPRA CCCCCCCEEEECCCH	17.62	28857561
150	Phosphorylation	RAQAAGSSVLRELHT CCCCCCHHHHHHHHC	25.01	28555341
160	Phosphorylation	RELHTADSVVNGSAQ HHHHCCCHHCCCCCC	26.04	28348404
179	Phosphorylation	KELEREESGAAESPA HHHHHHHCCCCCCCC	29.04	29255136
184	Phosphorylation	EESGAAESPALVTPD HHCCCCCCCCEECCC	15.67	29255136
189	Phosphorylation	AESPALVTPDSEKSA CCCCCEECCCCHHHH	23.41	30576142
192	Phosphorylation	PALVTPDSEKSAKHG CCEECCCCHHHHCCC	48.40	29978859
194	Ubiquitination	LVTPDSEKSAKHGSG EECCCCHHHHCCCCC	60.71	29967540
197	Ubiquitination	PDSEKSAKHGSGAFY CCCHHHHCCCCCCCC	56.44	-
200	Phosphorylation	EKSAKHGSGAFYSPE HHHHCCCCCCCCCHH	27.02	22617229
204	Phosphorylation	KHGSGAFYSPELLEA CCCCCCCCCHHHHHH	23.84	28464451
205	Phosphorylation	HGSGAFYSPELLEAL CCCCCCCCHHHHHHH	12.87	28464451
314	Phosphorylation	LRFTRPLTMAELSRL CCCCCCCCHHHHHHH	19.61	24505115
327	Phosphorylation	RLRRQFISYTKMHPN HHHHHHHHHHCCCCC	28.21	22210691
328	Phosphorylation	LRRQFISYTKMHPNN HHHHHHHHHCCCCCC	12.93	22210691

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of KTI12_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KTI12_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of KTI12_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of KTI12_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASSSPECTROMETRY.
PubMed: 19690332

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASSSPECTROMETRY.
PubMed: 18669648